The Mechanisms of Alpha-Amylase Inhibition by Flavan-3-Ols and the Possible Impacts of Drinking Green Tea on Starch Digestion

Autor: Desseaux, Veronique, Stocker, Pierre, Brouant, Pierre, Ajandouz, El Hassan, Health, Nutrition
Přispěvatelé: Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie Radicalaire (ICR), Aix Marseille Université (AMU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Zdroj: Journal of Food Science
Journal of Food Science, Wiley, 2018, 83 (11), pp.2858-2865. ⟨10.1111/1750-3841.14353⟩
Journal of Food Science, 2018, 83 (11), pp.2858-2865. ⟨10.1111/1750-3841.14353⟩
ISSN: 0022-1147
1750-3841
Popis: International audience; Many studies have shown that flavan-3-ols inhibit mammalian alpha-amylases but the published IC 50 and K i values vary up to a thousand times. We therefore tested the effects of 6 pure flavan-3-ols-abundant in green tea-on the activity of pure porcine pancreatic alpha-amylase (PPA) under steady-state kinetic conditions. We used both amylose and maltopentaose as substrates, along with spectrophotometry and chromatography as analytical tools, respectively. A Docking approach was also used to probe the interaction between PPA and each flavan-3-ol. The results showed that the 6 flavan-3-ols inhibit amylose hydrolysis with K i comprised between 7 and 34 μM, according to a mixed inhibition profile for gallocatechin gallate, and a competitive inhibition profile for the 5 other flavanols. Only the galloyl-containing flavan-3-ols inhibited the maltopentaose hydrolysis with a K i of about 30 μM according to a noncompetitive profile. We conclude that dietary flavan-3-ols could inhibit starch digestion nonnegligibly. The results of the docking trials were concordant with the kinetic data and have noticeably revealed that the cis-flavan-3-ols epigallocatechin gallate and epicatechin gallate bind similarly to PPA, involving π-stacking with Trp59.
Databáze: OpenAIRE
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